7tfo

Cryo-EM structure of HIV-1 Env trimer BG505 SOSIP.664 in complex with CD4bs antibody Ab1573

Method: ELECTRON MICROSCOPY Dmax: 144.4 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Envelope glycoprotein BG505 SOSIP.664 - gp120

Human immunodeficiency virus 1

UniProt A0A6H1VH54

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 12 其他Polymer 5 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 30–508 Chain B; UniProt 30–508 Chain C; UniProt 30–508 Not recorded CD4 binding site antibody Ab1573 - Fab heavy chain × 3 CD4 binding site antibody Ab1573 - Fab light chain × 3 Envelope glycoprotein BG505 SOSIP.664 - gp41 × 3 (Q2N0S6) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A6H1VH54_9PLVG
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–479; UniProt 30–508 Author chain B; PDBConstruct 1–479; UniProt 30–508 Author chain C; PDBConstruct 1–479; UniProt 30–508

Envelope glycoprotein BG505 SOSIP.664 - gp41

Human immunodeficiency virus 1

UniProt Q2N0S6

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 12 其他Polymer 5 PDB declaration: dodecameric(12) Consistent with protein copy count Chain X; UniProt 509–661 Chain Y; UniProt 509–661 Chain Z; UniProt 509–661 Fragment:UNP residues 509-661 Envelope glycoprotein BG505 SOSIP.664 - gp120 × 3 (A0A6H1VH54) CD4 binding site antibody Ab1573 - Fab heavy chain × 3 CD4 binding site antibody Ab1573 - Fab light chain × 3 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

186 other PDB entries and 199 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q2N0S6_9HIV1
Isoform
PDB entities 4
Chains and sequence ranges Author chain X; PDBConstruct 1–153; UniProt 509–661 Author chain Y; PDBConstruct 1–153; UniProt 509–661 Author chain Z; PDBConstruct 1–153; UniProt 509–661

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 7tfo

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7tfo
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7tfo
Deposition date deposition_date2022-01-06
Structure title titleCryo-EM structure of HIV-1 Env trimer BG505 SOSIP.664 in complex with CD4bs antibody Ab1573
Keywords keywords;Cryo-EM structure of the trimeric HIV-1 Env ecto-domain BG505 SOSIP.664 in complex with CD4 binding site antibody Ab1573, VIRAL PROTEIN, VIRAL PROTEIN-IMMUNE SYSTEM complex ;; VIRAL PROTEIN/IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier47.00
Radius of gyration Rg (electron density) rg_electron46.08
Forward intensity I(0) i0949793000.00
Molecular weight molecular_weight252960.0 kDa
Excluded volume excluded_volume315350 ų
Envelope volume envelope_volume447530 ų
Hydration-shell volume shell_volume79290 ų
Envelope diameter envelope_diameter146.9
Shell Rg shell_rg52.49
Envelope Rg envelope_rg44.67
Shape Rg shape_rg46.08
Total Rg total_rg46.35
Total atoms total_atoms17774
Residues n_residues2283
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax144.4
Rg (real space) rg_real46.63
Rg uncertainty (real space) rg_real_error0.97
I(0) (real space) i0_real9.4980e+08
I(0) uncertainty (real space) i0_real_error1.6780e+07
Rg (reciprocal space) rg_reciprocal47.00
I(0) (reciprocal space) i0_reciprocal950200000.0000
Solution quality estimate total_estimate0.8940
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary67.9
Skewness Skewness skewness-0.035
Kurtosis Kurtosis kurtosis-0.631
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha77050000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.914; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.975; Smooth: 0.901

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)